Commercial gigahertz-class NMR magnets

Nuclear Magnetic Resonance (NMR) spectroscopy is a wide-spread analytical technique which is used in a large range of different fields, such as quality control, food analysis, material science and structural biology. In the widest sense, NMR is an analytical technique to determine the structure of molecules. At the time of writing this manuscript, commercial NMR spectrometers with a proton resonance frequency ≥ 900 MHz are only available from Bruker. In 2019, Bruker installed the first 1.1 GHz (25.8 T) NMR spectrometer at the St. Jude Children Research Hospital in Memphis, Tennessee, followed by the installation of the first 1.2 GHz (28.2 T) NMR spectrometer at the University of Florence in Italy in 2020. These were the first commercial NMR spectrometers operating at magnetic fields in excess of what can be achieved with conventional low temperature superconductors, and which depend on high temperature superconductors to generate the required magnetic field. In this paper, the requirements on commercial NMR magnets are discussed and the history of high-field NMR magnets is reviewed. Bruker’s R&D program for 1.1 and 1.2 GHz NMR magnets and spectrometers will be described, and some of the key properties of these first commercial NMR magnets with high-temperature superconductors are reported.

Biomolecular solid-state NMR spectroscopy at 1200 MHz: the gain in resolution

Progress in NMR in general and in biomolecular applications in particular is driven by increasing magnetic-field strengths leading to improved resolution and sensitivity of the NMR spectra. Recently, persistent superconducting magnets at a magnetic field strength (magnetic induction) of 28.2 T corresponding to 1200 MHz proton resonance frequency became commercially available. We present here a collection of high-field NMR spectra of a variety of proteins, including molecular machines, membrane proteins, viral capsids, fibrils and large molecular assemblies. We show this large panel in order to provide an overview over a range of representative systems under study, rather than a single best performing model system. We discuss both carbon-13 and proton-detected experiments, and show that in 13C spectra substantially higher numbers of peaks can be resolved compared to 850 MHz while for 1H spectra the most impressive increase in resolution is observed for aliphatic side-chain resonances.

Biomolecular solid-state NMR spectroscopy at highest field: the gain in resolution at 1200 MHz

Progress in NMR in general and in biomolecular applications in particular is driven by increasing magnetic-field strengths leading to improved resolution and sensitivity of the NMR spectra. Recently, persistent superconducting magnets at a magnetic field strength (magnetic induction) of 28.2 T corresponding to 1200 MHz proton resonance frequency became commercially available. We present here a collection of high-field NMR spectra of a variety of proteins, including molecular machines, membrane proteins and viral capsids and others. We show this large panel in order to provide an overview over a range of representative systems under study, rather than a single best performing model system. We discuss both carbon-13 and proton-detected experiments, and show that in 13C spectra substantially higher numbers of peaks can be resolved compared to 850 MHz while for 1H spectra the most impressive increase in resolution is observed for aliphatic side-chain resonances.